ID A0A0V0WL27_9BILA Unreviewed; 508 AA.
AC A0A0V0WL27;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE Short=Katanin p60 subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE AltName: Full=p60 katanin {ECO:0000256|HAMAP-Rule:MF_03023};
GN Name=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023,
GN ECO:0000313|EMBL:KRX76463.1};
GN ORFNames=T06_14410 {ECO:0000313|EMBL:KRX76463.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX76463.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX76463.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX76463.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in
CC an ATP-dependent manner. Microtubule severing may promote rapid
CC reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation.
CC {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03023};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules,
CC which promote homooligomerization. ATP-dependent microtubule severing
CC is stimulated by interaction with KATNB1. {ECO:0000256|HAMAP-
CC Rule:MF_03023}.
CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be
CC promoted by interaction with microtubules. Interacts with KATNB1, which
CC may serve as a targeting subunit. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predominantly
CC cytoplasmic. Also localized to the interphase centrosome and the
CC mitotic spindle poles. Enhanced recruitment to the mitotic spindle
CC poles requires microtubules and interaction with KATNB1.
CC {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX76463.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDK01000100; KRX76463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WL27; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR CDD; cd21748; Kp60-NTD; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR048611; KATNA1_MIT.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Spast_Vps4_C.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF19; KATANIN P60 ATPASE-CONTAINING SUBUNIT A1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF21126; KATNA1_MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03023};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03023};
KW Microtubule {ECO:0000256|HAMAP-Rule:MF_03023};
KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03023};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 260..400
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 97..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
SQ SEQUENCE 508 AA; 56935 MW; 0ADB709F6E8161C3 CRC64;
MNYDELCFHI QNGRDSASLG LYSAARTSYG KALHLINGFL ATCTDVERRE QWQSAIQTIN
VELSTVNSIT ELLEDLSRSS ASRNGCAVES LVFNIEENKP WPSPTNVEKK TSSVLLTRST
NRKQHVTEFE KEKQRASSNK LFDVPRSGAN SSGNSRRRLV NSNESTPNRP PIKKNTSAAG
QKSANRPQSS EDQPVEVEKK FDSSNCDKEL VEILERDIVL RNPNIHWSDI AGLTEAKNLL
HEAVVLPRIM PMFFKGLRSP WRGVCMFGPP GTGKTMLAKA VATECNTTFF NVSASTLTSK
YRGDSEKLVR LLFEMARFYA PSTIFIDEID SICSRRGSES EHEASRRVKS ELLIQMDGVI
SSNPNSAAGV LVLAATNFPW DLDEALRRRL EKRVFIPLPD ASCRLEMLKL NLRDLKLADD
LDLAEIAEKL EGYSGADLTN VCRDAAMMSM RQRIAGLEMD EIARLHAEDL DLPITRQDFV
EALARSSKSV SQQDLDKYEK WMKEFGSI
//
